Kinetics of the reduction of neptunium(VI) by dicarboxylic acids

1984 ◽  
Vol 23 (15) ◽  
pp. 2351-2354 ◽  
Author(s):  
L. F. Rao ◽  
G. R. Choppin
Keyword(s):  
Dicarboxylic Acids ◽  
Kinetics Of

Kinetics of the reactions of nickel(II) ion with dicarboxylic acids in dioxan–water

1980 ◽  
pp. 41-45 ◽  
Author(s):  
Gioacchina Arcoleo ◽  
F. Paolo Cavasino ◽  
Emanuele Di Dio ◽  
Carmelo Sbriziolo
Keyword(s):  
Dicarboxylic Acids ◽  
Kinetics Of

Kinetics of complex formation between some dicarboxylic acids and iron(III) in aqueous solution

1977 ◽  
Vol 22 ◽  
pp. 61-67 ◽  
Author(s):  
G. Calvaruso ◽  
F.P. Cavasino ◽  
E.Di Dio ◽  
R. Triolo
Keyword(s):  
Aqueous Solution ◽  
Complex Formation ◽  
Dicarboxylic Acids ◽  
Kinetics Of

Reaction mechanisms and kinetics of xylo-oligosaccharide hydrolysis by dicarboxylic acids

AIChE Journal ◽  
2012 ◽  
Vol 59 (1) ◽  
pp. 188-199 ◽  
Author(s):  
Youngmi Kim ◽  
Thomas Kreke ◽  
Michael R. Ladisch
Keyword(s):  
Reaction Mechanisms ◽  
Dicarboxylic Acids ◽  
Kinetics Of ◽  
Oligosaccharide Hydrolysis

Kinetics of the thermal decomposition of dicarboxylic acids

1994 ◽  
Vol 239 ◽  
pp. 51-59 ◽  
Author(s):  
K. Muraishi ◽  
Y. Suzuki ◽  
A. Kikuchi
Keyword(s):  
Thermal Decomposition ◽  
Dicarboxylic Acids ◽  
Kinetics Of

P.85 Kinetics of triglycerides of dicarboxylic acids in rats

1995 ◽  
Vol 14 ◽  
pp. 57
Author(s):  
E. Capristo ◽  
G. Mingrone ◽  
G. Benedetti ◽  
A.V. Greco ◽  
M. Castagneto ◽  
...  
Keyword(s):  
Dicarboxylic Acids ◽  
Kinetics Of

scholarly journals Regulation of phosphoenolpyruvate carboxylase of Zea mays by metabolites

1973 ◽  
Vol 131 (3) ◽  
pp. 451-458 ◽  
Author(s):  
K. F. Wong ◽  
D. D. Davies
Keyword(s):  
Zea Mays ◽  
Phosphoenolpyruvate Carboxylase ◽  
Competitive Inhibition ◽  
Energy Charge ◽  
Dicarboxylic Acids ◽  
Ph Optimum ◽  
Km Value ◽  
Sugar Phosphates ◽  
Kinetics Of ◽  
Kinetics Of Inhibition

Crude preparations of phosphoenolpyruvate carboxylase obtained from aetiolated seedlings of Zea mays are unstable but can be stabilized with glycerol. At the pH optimum of 8.3, the Km value for phosphoenolpyruvate is 80μm. When assayed at 30°C, the enzyme shows normal Michaelis–Menten kinetics, but when assayed at 45°C sigmoid kinetics are exhibited. At pH7.0 the enzyme is inhibited by a number of dicarboxylic acids and by glutamate and aspartate. d and l forms of the hydroxy acids and amino acids are inhibitory and the kinetics approximate to simple non-competitive inhibition. The same compounds produce less inhibition at pH7.6 than at pH7.0 and the kinetics of inhibition are more complex. The enzyme is activated by Pi, by SO42- and by a number of sugar phosphates. Maximum activation occurs at acid pH values, where enzyme activity is lowest. The enzyme is activated by AMP and inhibited by ADP and ATP so that the response to energy charge is of the R type and is thus at variance with Atkinson's (1968) concept of energy charge. The physiological significance of the response to metabolites is discussed.

Study of the kinetics of polycondensation of the salts of dicarboxylic acids and diamines in solution

1987 ◽  
Vol 29 (4) ◽  
pp. 823-828
Author(s):  
A.P. Khardin ◽  
I.A. Novakov ◽  
S.S. Radchenko ◽  
I.A. Kulev ◽  
B.S. Orlinson ◽  
...  
Keyword(s):  
Dicarboxylic Acids ◽  
Kinetics Of
Sign in / Sign up

Export Citation Format

Share Document